Abstract
Peptides have been shown to undergo intrinsic lipidation reactions in lipid membranes (http://dx.doi.org/10.1016/j.jmb.2013.07.013), involving acyl transfer from lipid constituents of the membrane to acceptor sites on the peptide. The physical properties of the membrane that promote this process have been investigated and are rationalized in terms of the rate determining step in the process and the curvature modulus of the membrane. The lipidation by-products, lyso-lipids, may also serve as acyl group donors for further lipidation. Intrinsic lipidation is not restricted to peptides: proteins and small molecules also undergo the process. We have examined the lipidation profiles of aquaporin-0 and shown that it can be accounted for with knowledge of the fatty acyl composition of lens membranes, thereby supporting the hypothesis that their lipidation arises from membrane lipid precursors. Current work to understand the factors that dictate this reactivity, and the consequences of lipidation, will be presented.
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